Structure-function analysis of PrsA reveals roles for the parvulin-like and flanking N- and C-terminal domains in protein folding and secretion in Bacillus subtilis.
D001412:Bacillus subtilis / Q000737:chemistry* / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry; D020134:Catalytic Domain; D008074:Lipoproteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology*; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology*; D016297:Mutagenesis, Site-Directed; D000072340:NIMA-Interacting Peptidylprolyl Isomerase; D019696:Peptidylprolyl Isomerase / Q000737:chemistry; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000378:metabolism*
D001426:Bacterial Proteins; D008074:Lipoproteins; D008565:Membrane Proteins; D000072340:NIMA-Interacting Peptidylprolyl Isomerase; D011506:Proteins; C082160:prsA protein, bacteria; D019696:Peptidylprolyl Isomerase